ID A0A3Q0F4N1_VIGRR Unreviewed; 975 AA.
AC A0A3Q0F4N1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN Name=LOC106774350 {ECO:0000313|RefSeq:XP_022637569.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022637569.1};
RN [1] {ECO:0000313|RefSeq:XP_022637569.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022637569.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases to synthesize the diphosphate group-containing inositol
CC pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC of cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC hexakisphosphate (InsP6). {ECO:0000256|RuleBase:RU365032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC ChEBI:CHEBI:456216; EC=2.7.4.24;
CC Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|RuleBase:RU365032}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609,
CC ECO:0000256|RuleBase:RU365032}.
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DR RefSeq; XP_022637569.1; XM_022781848.1.
DR AlphaFoldDB; A0A3Q0F4N1; -.
DR Proteomes; UP000087766; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:InterPro.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.11950; -; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF26; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 9..117
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
SQ SEQUENCE 975 AA; 110415 MW; D733EB43EF8A4F61 CRC64;
MAVALADKVK IGVCVMEKKV KCHSEVFSAP MGQIFDRLQA FGEFEVIHFG DKVILEEPIE
SWPICDCLIA FYSSGYPLEK AEAYAALRKF TGPKTTHALG CRPFVVNELE PQHLLHDRRK
VYEVGNRSSE FHPDVRRVRR EGSYIYEEFM PTGGTDVKVY TVGPEYAHAE ARKSPVVDGV
VMRNPDGKEV RYPVLLSPAE KEMARDVCIA FSQAVCGFDL LRSQGRSYVC DVNGWSFVKN
SYKYYDDSAC VLRKMLLDAK APHLSSVVPP TLPWKVNELT QPSEPLTREP LTRQGSGING
TFGQSEELRC VIAVIRHGDR TPKQKVKLKV TEEKLLNLML KYNGGRPKSE TKLKSAVQLQ
DLLDATRMLV PRTRPDSDSE AEDVDHAEKL RQVKVVLEEG GHFSGIYRKV QLKPLKWIKV
TKGNGEIEEQ PVEALMILKY GGVLTHAGRK QAEELGRYFR NKMYPGEGTG LLRLHSTYRH
DMKIYSSDEG RVQMSAAAFA KGLLDLEGQL TPILVSLVSK DSSMLDGLEN ASFEMDEAKA
RLNEIITCKA TTSDTNGSSE FPWTVDGAGL PPNASELLST LVKLTKKVTE QVRLLAKDEN
DKLTERNLYD IVPPYDQANA LGKTNIDVDR IAAGLPCGSE GFLLMYARWK KLETDLYNER
KERYDITQIP DVYDSCKYDL LHNAHLNLEG LDELFKVAQM LADGVIPNEY GINPKQKLKI
GAKVARRLLG KLLIDLRNTR EEAINVIKNN EDLSLSEKIK KDAEAKSKLF HKNDEIDQDD
DDDKETKYRL DPKYANVKTP DRHVRTRLYF TSESHIHSLM NVLRYCNLDE SLQEEEGLVC
HSALERLSKT KELDYMSHIV LRMFENTEVA LEDPKRYRIE LSYSRGADLS PLEKEGSECT
LHQEHTLPIM GPERLQQVGS YLTLETMENM IRPFAMPAED FPPTPAGFSG YFSKSVLDRL
VNLWPFHRQF SNLGK
//
